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Background
TIMP metallopeptidase inhibitor 2 also known as TIMP2, which belongs to the protease inhibitor I35 (TIMP) family. This family protein are natural inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. The TIMP family encompasses four members (TIMP1, TIMP2, TIMP3, TIMP4), and they inhibit most MMPs by forming non-covalent binary complex. In addition to an inhibitory role against metalloproteinases, TIMP2 has a unique role among TIMP family members in its ability to directly suppress the proliferation of endothelial cells. As a result, TIMP-2 may be critical to the maintenance of tissue homeostasis by suppressing the proliferation of quiescent tissues in response to angiogenic factors, and by inhibiting protease activity in tissues undergoing remodelling of the extracellular matrix.
Source
Recombinant Human CSC-21K /TIMP2 Protein (rhTIMP2) Cys 27 - Pro 220 (Accession # NP_003246.1) was produced in human 293 cells (HEK293).
Molecular Characterization
rhTIMP2, fused with 6×His tag at the C-terminus, has a calculated MW of 22.6 kDa. The predicted N-terminus is Cys 27. DTT-reduced Protein migrates as 22 kDa.
Endotoxin
Less than 1.0 EU per μg of the rhTIMP2 by the LAL method.
Purity
>95% as determined by SDS-PAGE.
Formulation
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, 0.05% Brij-35, pH 7.5. Normally Mannitol or Trehalose are added as protectants before lyophilization.
(1) Stetler-Stevenson W.G., et al., 1989, J. Biol. Chem. 264:17374-17378.
(2) Goldberg G.I., et al., 1989, Proc. Natl. Acad. Sci. U.S.A. 86:8207-8211.
(3) Chattopadhyay N., et al., 2001, J. Cancer Res. Clin. Oncol. 127:653-658.
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